9jxp

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Current revision (07:17, 27 August 2025) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 9jxp is ON HOLD until Paper Publication
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==Cryo-EM structure of human XPR1-R570L==
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<StructureSection load='9jxp' size='340' side='right'caption='[[9jxp]], [[Resolution|resolution]] 3.53&Aring;' scene=''>
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Authors: Wang, X., Bai, Z., Wallis, C., Wang, H., Han, Y., Jin, R., Lei, M., Gu, C., Jessen, H., Shears, S., Sun, Y., Corry, B., Zhang, Y.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9jxp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9JXP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9JXP FirstGlance]. <br>
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Description: Cryo-EM structure of human XPR1-R570L
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.53&#8491;</td></tr>
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[[Category: Unreleased Structures]]
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9jxp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9jxp OCA], [https://pdbe.org/9jxp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9jxp RCSB], [https://www.ebi.ac.uk/pdbsum/9jxp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9jxp ProSAT]</span></td></tr>
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[[Category: Lei, M]]
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</table>
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[[Category: Corry, B]]
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== Disease ==
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[[Category: Bai, Z]]
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[https://www.uniprot.org/uniprot/S53A1_HUMAN S53A1_HUMAN] Bilateral striopallidodentate calcinosis. The disease is caused by variants affecting the gene represented in this entry.
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[[Category: Wang, X]]
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== Function ==
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[[Category: Wallis, C]]
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[https://www.uniprot.org/uniprot/S53A1_HUMAN S53A1_HUMAN] Inorganic ion transporter that mediates phosphate ion export across plasma membrane. Plays a major role in phosphate homeostasis, preventing intracellular phosphate accumulation and possible calcium phosphate precipitation, ultimately preserving calcium signaling. The molecular mechanism of phosphate transport, whether electrogenic, electroneutral or coupled to other ions, remains to be elucidated (By similarity) (PubMed:23791524, PubMed:25938945, PubMed:31043717). Binds inositol hexakisphosphate (Ins6P) and similar inositol polyphosphates, such as 5-diphospho-inositol pentakisphosphate (5-InsP7), important intracellular signaling molecules involved in regulation of phosphate flux (PubMed:27080106).[UniProtKB:Q9Z0U0]<ref>PMID:23791524</ref> <ref>PMID:25938945</ref> <ref>PMID:27080106</ref> <ref>PMID:31043717</ref>
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[[Category: Han, Y]]
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== References ==
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[[Category: Shears, S]]
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<references/>
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[[Category: Sun, Y]]
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__TOC__
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[[Category: Wang, H]]
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</StructureSection>
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[[Category: Jessen, H]]
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[[Category: Homo sapiens]]
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[[Category: Gu, C]]
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[[Category: Large Structures]]
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[[Category: Zhang, Y]]
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[[Category: Bai Z]]
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[[Category: Jin, R]]
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[[Category: Corry B]]
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[[Category: Gu C]]
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[[Category: Han Y]]
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[[Category: Jessen H]]
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[[Category: Jin R]]
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[[Category: Lei M]]
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[[Category: Shears S]]
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[[Category: Sun Y]]
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[[Category: Wallis C]]
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[[Category: Wang H]]
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[[Category: Wang X]]
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[[Category: Zhang Y]]

Current revision

Cryo-EM structure of human XPR1-R570L

PDB ID 9jxp

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